Qualitative and Quantitative Variants of Human Phosphoglucose Isomerase

Welch, S.G.

doi:10.1159/000152439

Cited by 33 publications

(8 citation statements)

References 5 publications

(11 reference statements)

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“…Since this discovery there have been reports of rare genetically determined variants or variants with low catalytic activities from various populations of the world Fitch et al, 1968;Paglia et al, 1969;Shinoda, 1970; Tariverdian et aI., 1970;Welch 1971;Luan Eng and Welch, 1972;Sanpitak et aL, 1973; Nakashima et aI., 1973;Isacchi et al, 1979), most of which concerns the sporadic occurrence of one or two of the nine heterozygotic types originally described in addition to the usual homozygous phenotype PGI-1. The exceptions are the heterozygous phenotypes PGI 3-1 and 4-1 which are of particular interest in Asiatic populations.…”

Section: Discussionmentioning

confidence: 99%

“…The exceptions are the heterozygous phenotypes PGI 3-1 and 4-1 which are of particular interest in Asiatic populations. In both the studies from London (Detter et al, 1968;Welch, 1971) the Asiatic Indians showed an appreciable frequency of the variant PGI 3-1 and subsequent studies of indigenous samples confirmed that the PGI a allele attains polymorphic frequencies in certain populations of India. Indeed, the relatively high frequency of this allele led to the detection of the homozygous phenotype PGI-3 (Papiha et aL, 1974).…”

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Population genetic study of red cell enzyme phosphoglucose isomerase in India

Papiha

Chahal

1984

Jap J Human Genet

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SummaryThe distribution of red cell enzyme phosphoglucose isomerase was studied by starch gel electrophoresis in 27 different endogamous groups of India. Forty one electrophoretic variants belonging to four out of the nine known heterozygote types and one rare homozygous variant (PGI-3) were found. Comparison of the results with in India and certain other populations showed that PGI is certainly another useful genetic parameter for the study of population diversity in Asia.Inherited variation of the enzyme phosphoglucose isomerase [PGI; o~-D-glucose 6-phosphate ketol isomerase; EC 5.3.1.9] was initially described by Detter et al. (1968), the enzyme being referred to as phosphohexose isomerase. Since this discovery there have been reports of rare genetically determined variants or variants with low catalytic activities from various populations of the world Fitch et al., 1968;Paglia et al., 1969;Shinoda, 1970; Tariverdian et aI., 1970;Welch 1971;Luan Eng and Welch, 1972;Sanpitak et aL, 1973; Nakashima et aI., 1973;Isacchi et al., 1979), most of which concerns the sporadic occurrence of one or two of the nine heterozygotic types originally described in addition to the usual homozygous phenotype PGI-1. The exceptions are the heterozygous phenotypes PGI 3-1 and 4-1 which are of particular interest in Asiatic populations. In both the studies from London (Detter et al., 1968;Welch, 1971) the Asiatic Indians showed an appreciable frequency of the variant PGI 3-1 and subsequent studies of indigenous samples confirmed that the PGI a allele attains polymorphic frequencies in certain populations of India. Indeed, the relatively high frequency of this allele led to the detection of the homozygous phenotype PGI-3 (Papiha et aL, 1974). Ishimoto and Kuwata (1974) compiled the PGI studies in Japan and showed that in Japanese PGI 4-1 variant is more frequent than the other known heterozygous variants. This relatively high frequency of the PGI 4 allele in Japan consistent with the previous studies of Shinoda (1970), also led to the finding of a rare

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Section: Discussionmentioning

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confidence: 85%

Population genetic study of red cell enzyme phosphoglucose isomerase in India

Papiha

Chahal

1984

Jap J Human Genet

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“…It interconverts glucose 6-phosphate and fructose 6-phosphate, hence plays a central role in both the glycolysis and the gluconeogenesis pathways. PGI deficiency in humans is an autosomal recessive genetic disorder that has the typical manifestation of nonspherocytic hemolytic anemia of variable clinical expression (1,2). The serum activity of human PGI serves as a tumor marker in cancer patients (3,4) and elevation in PGI activity is closely correlated with metastasis (5,6).…”

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The Crystal Structure of Phosphoglucose Isomerase/Autocrine Motility Factor/Neuroleukin Complexed with Its Carbohydrate Phosphate Inhibitors Suggests Its Substrate/Receptor Recognition

Chou¹,

Sun²,

Meng³

et al. 2000

Journal of Biological Chemistry

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Phosphoglucose isomerase catalyzes the reversible isomerization of glucose 6-phosphate to fructose 6-phosphate. In addition, phosphoglucose isomerase has been shown to have functions equivalent to neuroleukin, autocrine motility factor, and maturation factor. Here we present the crystal structures of phosphoglucose isomerase complexed with 5-phospho-D-arabinonate and N-bromoacetylethanolamine phosphate at 2.5-and 2.3-Å resolution, respectively. The inhibitors bind to a region within the domains' interface and interact with a histidine residue (His 306 ) from the other subunit. We also demonstrated that the inhibitors not only affect the enzymatic activity of phosphoglucose isomerase, but can also inhibit the autocrine motility factor-induced cell motility of CT-26 mouse colon tumor cells. These results indicate that the substrate and the receptor binding sites of phosphoglucose isomerase and autocrine motility factor are located within close proximity to each other. Based on these two complex structures, together with biological and biochemical results, we propose a possible isomerization mechanism for phosphoglucose isomerase.Phosphoglucose isomerase (PGI) 1 (EC 5.3.1.9), a glycolytic enzyme, is an essential enzyme in all tissues. It interconverts glucose 6-phosphate and fructose 6-phosphate, hence plays a central role in both the glycolysis and the gluconeogenesis pathways. PGI deficiency in humans is an autosomal recessive genetic disorder that has the typical manifestation of nonspherocytic hemolytic anemia of variable clinical expression (1, 2). The serum activity of human PGI serves as a tumor marker in cancer patients (3, 4) and elevation in PGI activity is closely correlated with metastasis (5, 6). In addition to its essential role in carbohydrate metabolism in the cytoplasm, PGI also functions as neuroleukin (NLK) (7-9), autocrine motility factor (AMF) (10, 11), and maturation factor (MF) (12).NLK is a neurotrophic growth factor that promotes the survival of spinal and sensory neurons (13). Interestingly, PGI and NLK have previously been reported to have differential induction capabilities for certain neurons (9). AMF, a new class of cytokines, can stimulate cell migration in vitro and metastasis in vivo (10, 14 -16). Amino acid sequencing and immunological cross-reactivity experiments suggest that mouse AMF is identical or closely related to PGI/NLK (10). MF is capable of mediating the differentiation of human myeloid leukemic HL-60 cells to terminal monocytic cells, and apparently a high degree of homology exists between the MF of myeloid leukemia cells and PGI or NLK (12).It was previously suggested that PGI may recognize a sugarcontaining molecule(s) at the cell surface (7) and that NLK binds to the cell surface in a carbohydrate-dependent manner utilizing a PGI-like structure. Watanabe (10, 16) also pointed out that AMF (PGI/NLK/MF) may contain a PGI-like structure and initiates signal transduction by interacting with the carbohydrate side chains of the extracellular domain of the AMF receptor (AMF...

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“…PGI deficiency in humans leads to nonspherocytic hemolytic disease (1,2). In addition, the serum activity of PGI has been established as a tumor marker in human cancer patients (3,4), and elevation in PGI activity is closely correlated with metastasis (5,6).…”

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confidence: 99%

The crystal structure of a multifunctional protein: Phosphoglucose isomerase/autocrine motility factor/neuroleukin

Sun

Chou

Chen³

et al. 1999

Proc. Natl. Acad. Sci. U.S.A.

106

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Phosphoglucose isomerase (PGI) plays a central role in both the glycolysis and the gluconeogenesis pathways. We present here the complete crystal structure of PGI from Bacillus stearothermophilus at 2.3-Å resolution. We show that PGI has cell-motility-stimulating activity on mouse colon cancer cells similar to that of endogenous autocrine motility factor (AMF). PGI can also enhance neurite outgrowth on neuronal progenitor cells similar to that observed for neuroleukin. The results confirm that PGI is neuroleukin and AMF. PGI has an open twisted ␣͞␤ structural motif consisting of two globular domains and two protruding parts. Based on this substrate-free structure, together with the previously published biological, biochemical, and modeling results, we postulate a possible substrate-binding site that is located within the domains' interface for PGI and AMF. In addition, the structure provides evidence suggesting that the top part of the large domain together with one of the protruding loops might participate in inducing the neurotrophic activity.

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Qualitative and Quantitative Variants of Human Phosphoglucose Isomerase

Cited by 33 publications

References 5 publications

Population genetic study of red cell enzyme phosphoglucose isomerase in India

Population genetic study of red cell enzyme phosphoglucose isomerase in India

The Crystal Structure of Phosphoglucose Isomerase/Autocrine Motility Factor/Neuroleukin Complexed with Its Carbohydrate Phosphate Inhibitors Suggests Its Substrate/Receptor Recognition

The crystal structure of a multifunctional protein: Phosphoglucose isomerase/autocrine motility factor/neuroleukin

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